Mandelate racemase interconverts the enantiomers of mandelate through an exzymatic base extraction of the alpha-hydrogen as a proton. One way to study the mechanism of this reaction is visualizing the enzyme's active site through the x-ray crystallographic data. In collaboration with Professor Greg Petsko and coworkers, crystals of the native enzyme, enzyme-substrate complex and mutant enzymes were produced and the data was refined beyond 2.5 Angstroms resolution. The UCSF Computer Graphics Laboratory is invaluable in helping me to visualize these crystallographic data sets. From this study, further site directed mutagenesis and future work will be proposed to test the importance of active site residues to catalysis. The UCSF CGL provides an indispensable service necessary for this research.